FH1/FH2 domain-containing protein 1 is a protein that in humans is encoded by the FHOD1gene.[1][2][3]
This gene encodes a protein which is a member of the formin/diaphanous family of proteins. The gene is ubiquitously expressed but is found in abundance in the spleen. The encoded protein has sequence homology to diaphanous and formin proteins within the Formin Homology (FH)1 and FH2 domains. It also contains a coiled-coil domain, a collagen-like domain, two nuclear localization signals, and several potential PKC and PKA phosphorylation sites. It is a predominantly cytoplasmic protein and is expressed in a variety of human cell lines.[3]
↑Westendorf JJ, Mernaugh R, Hiebert SW (Jul 1999). "Identification and characterization of a protein containing formin homology (FH1/FH2) domains". Gene. 232 (2): 173–82. doi:10.1016/S0378-1119(99)00127-4. PMID10352228.
↑Boehm MB, Milius TJ, Zhou Y, Westendorf JJ, Koka S (Aug 2005). "The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway". Biochem Biophys Res Commun. 335 (4): 1090–4. doi:10.1016/j.bbrc.2005.07.191. PMID16112087.
↑Westendorf, J J (Dec 2001). "The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element". J. Biol. Chem. United States. 276 (49): 46453–9. doi:10.1074/jbc.M105162200. ISSN0021-9258. PMID11590143.
Further reading
Westendorf JJ (2002). "The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element". J. Biol. Chem. 276 (49): 46453–9. doi:10.1074/jbc.M105162200. PMID11590143.
Koka S, Neudauer CL, Li X, et al. (2004). "The formin-homology-domain-containing protein FHOD1 enhances cell migration". J. Cell Sci. 116 (Pt 9): 1745–55. doi:10.1242/jcs.00386. PMID12665555.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID12665801.
Tojo H, Kaieda I, Hattori H, et al. (2004). "The Formin family protein, formin homolog overexpressed in spleen, interacts with the insulin-responsive aminopeptidase and profilin IIa". Mol. Endocrinol. 17 (7): 1216–29. doi:10.1210/me.2003-0056. PMID12677009.
Takeya R, Sumimoto H (2004). "Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation". J. Cell Sci. 116 (Pt 22): 4567–75. doi:10.1242/jcs.00769. PMID14576350.
Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID14667819.
Katoh M, Katoh M (2004). "Identification and characterization of human FHOD3 gene in silico". Int. J. Mol. Med. 13 (4): 615–20. doi:10.3892/ijmm.13.4.615. PMID15010865.
Wang Y, El-Zaru MR, Surks HK, Mendelsohn ME (2004). "Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells". J. Biol. Chem. 279 (23): 24420–6. doi:10.1074/jbc.M313823200. PMID15051728.
Westendorf JJ, Koka S (2004). "Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated actin dynamics". J. Cell. Biochem. 92 (1): 29–41. doi:10.1002/jcb.20031. PMID15095401.
Gill MB, Roecklein-Canfield J, Sage DR, et al. (2005). "EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation with CD21: formin interactions with the cytoplasmic domain of human CD21". J. Cell Sci. 117 (Pt 13): 2709–20. doi:10.1242/jcs.01113. PMID15138285.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID15146197.
Madrid R, Gasteier JE, Bouchet J, et al. (2005). "Oligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities". FEBS Lett. 579 (2): 441–8. doi:10.1016/j.febslet.2004.12.009. PMID15642356.
Gasteier JE, Schroeder S, Muranyi W, et al. (2005). "FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation". Exp. Cell Res. 306 (1): 192–202. doi:10.1016/j.yexcr.2005.02.006. PMID15878344.
Schönichen A, Alexander M, Gasteier JE, et al. (2006). "Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1". J. Biol. Chem. 281 (8): 5084–93. doi:10.1074/jbc.M509226200. PMID16361249.